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A common antigenic determinant found in two functionally unrelated toxins
The heat-stable enterotoxin ST Ib produced by enterotoxigenic E. coli strains shares a sequence homology with the sea snail neurotoxin, conotoxin GI. Rabbit antisera were raised against synthetic analogs of these toxins and to a six-residue peptide representing the region common to both toxins. Resu...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1984
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2187476/ https://www.ncbi.nlm.nih.gov/pubmed/6207263 |
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collection | PubMed |
description | The heat-stable enterotoxin ST Ib produced by enterotoxigenic E. coli strains shares a sequence homology with the sea snail neurotoxin, conotoxin GI. Rabbit antisera were raised against synthetic analogs of these toxins and to a six-residue peptide representing the region common to both toxins. Results from enzyme-linked immunosorbent assays indicate that the homologous region of both toxins represents part of their antigenic site. The lack of cross-reactivity exhibited by the six- residue common domain with serum directed against either toxin suggests that this region probably retains a similar conformation in the intact toxins but not in the isolated fragment. |
format | Text |
id | pubmed-2187476 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1984 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21874762008-04-17 A common antigenic determinant found in two functionally unrelated toxins J Exp Med Articles The heat-stable enterotoxin ST Ib produced by enterotoxigenic E. coli strains shares a sequence homology with the sea snail neurotoxin, conotoxin GI. Rabbit antisera were raised against synthetic analogs of these toxins and to a six-residue peptide representing the region common to both toxins. Results from enzyme-linked immunosorbent assays indicate that the homologous region of both toxins represents part of their antigenic site. The lack of cross-reactivity exhibited by the six- residue common domain with serum directed against either toxin suggests that this region probably retains a similar conformation in the intact toxins but not in the isolated fragment. The Rockefeller University Press 1984-10-01 /pmc/articles/PMC2187476/ /pubmed/6207263 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles A common antigenic determinant found in two functionally unrelated toxins |
title | A common antigenic determinant found in two functionally unrelated toxins |
title_full | A common antigenic determinant found in two functionally unrelated toxins |
title_fullStr | A common antigenic determinant found in two functionally unrelated toxins |
title_full_unstemmed | A common antigenic determinant found in two functionally unrelated toxins |
title_short | A common antigenic determinant found in two functionally unrelated toxins |
title_sort | common antigenic determinant found in two functionally unrelated toxins |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2187476/ https://www.ncbi.nlm.nih.gov/pubmed/6207263 |